RSKA_MYCUA
ID RSKA_MYCUA Reviewed; 232 AA.
AC A0PNM3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Anti-sigma-K factor RskA;
DE AltName: Full=Regulator of SigK;
DE AltName: Full=Sigma-K anti-sigma factor RskA;
GN Name=rskA; OrderedLocusNames=MUL_1399;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor SigK. ECF sigma factors are held in an inactive form by an
CC anti-sigma factor until released by regulated intramembrane proteolysis
CC (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. The membrane-spanning regulatory substrate protein is first
CC cut extracytoplasmically (site-1 protease, S1P), then within the
CC membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating the sigma
CC factor (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The cytosolic domain interacts with sigma factor SigK.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the anti-sigma-K factor family. {ECO:0000305}.
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DR EMBL; CP000325; ABL03942.1; -; Genomic_DNA.
DR RefSeq; WP_011739563.1; NC_008611.1.
DR AlphaFoldDB; A0PNM3; -.
DR SMR; A0PNM3; -.
DR STRING; 362242.MUL_1399; -.
DR EnsemblBacteria; ABL03942; ABL03942; MUL_1399.
DR GeneID; 64259506; -.
DR KEGG; mul:MUL_1399; -.
DR eggNOG; COG5343; Bacteria.
DR HOGENOM; CLU_075802_1_1_11; -.
DR OMA; VYQMWLI; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.10.1320; -; 1.
DR InterPro; IPR018764; Anti-sigma_K_RskA.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
DR Pfam; PF10099; RskA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..232
FT /note="Anti-sigma-K factor RskA"
FT /id="PRO_0000313837"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 232 AA; 23962 MW; 6A230AFC7EB20626 CRC64;
MTEPTDFQLL ELATPYALHA VSDEERLDIE RRLSAAPAPV AAAFDEEVRS VRETMSVVSA
ATAAQPPAEL RQALLAAAEP AQSRRQPRWR TAVFASAAAI AVGLGAFGLG VLTRPSASPT
VAEQVLAAPD VQTVSGRLGG GTATVMFSRD RNAGVLVMNN VPPPSPGTVY QMWLVDAKGP
TSAGTMGPTA VTPSTKATLT DLGDSTTLAF TVEPGTGSTK PTGTVLAELP LR